Q90YB1
Gene name |
LIG4 |
Protein name |
DNA ligase 4 |
Names |
DNA ligase IV, Polydeoxyribonucleotide synthase [ATP] 4 |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:418764 |
EC number |
6.5.1.1: Forming phosphoric ester bonds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q90YB1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q90YB1-F1 | Predicted | AlphaFoldDB |
No variants for Q90YB1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q90YB1 | |||||
No associated diseases with Q90YB1
9 regional properties for Q90YB1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | BRCT domain | 659 - 748 | IPR001357-1 |
| domain | BRCT domain | 811 - 912 | IPR001357-2 |
| domain | DNA ligase, ATP-dependent, N-terminal | 20 - 213 | IPR012308 |
| domain | DNA ligase, ATP-dependent, C-terminal | 481 - 593 | IPR012309 |
| domain | DNA ligase, ATP-dependent, central | 253 - 494 | IPR012310 |
| conserved_site | DNA ligase, ATP-dependent, conserved site | 276 - 284 | IPR016059-1 |
| conserved_site | DNA ligase, ATP-dependent, conserved site | 432 - 456 | IPR016059-2 |
| domain | DNA ligase IV domain | 755 - 787 | IPR021536 |
| domain | DNA Ligase 4, adenylation domain | 240 - 461 | IPR044125 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.5.1.1 | Forming phosphoric ester bonds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| DNA ligase IV complex | A eukaryotically conserved protein complex that contains DNA ligase IV and is involved in DNA repair by non-homologous end joining; in addition to the ligase, the complex also contains XRCC4 or a homolog, e.g. Saccharomyces Lif1p. |
| DNA-dependent protein kinase-DNA ligase 4 complex | A large protein complex which is involved in the repair of DNA double-strand breaks and, in mammals, V(D)J recombination events. It consists of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), the DNA end-binding heterodimer Ku, the nuclear phosphoprotein XRCC4 or a homolog thereof, and DNA ligase IV. |
| nonhomologous end joining complex | A protein complex that plays a role in DNA double-strand break repair via nonhomologous end joining. Such complexes typically contain a specialized DNA ligase (e.g. Lig4 in eukaryotes) and one or more proteins that bind to DNA ends. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA ligase (ATP) activity | Catalysis of the reaction: ATP + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + diphosphate + deoxyribonucleotide(n+m). |
| metal ion binding | Binding to a metal ion. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| cell cycle | The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division. |
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| DNA biosynthetic process | The biosynthetic process resulting in the formation of DNA. |
| DNA ligation involved in DNA repair | The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase, that contributes to DNA repair. |
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
| double-strand break repair via nonhomologous end joining | The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear. |
| immunoglobulin V(D)J recombination | The process in which immunoglobulin gene segments are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). For immunoglobulin heavy chains V, D, and J gene segments are joined, and for immunoglobulin light chains V and J gene segments are joined. |
| nucleotide-excision repair, DNA gap filling | Repair of the gap in the DNA helix by DNA polymerase and DNA ligase after the portion of the strand containing the lesion has been removed by pyrimidine-dimer repair enzymes. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASAPVLQPS | PKRTVASHVP | FADLCSTLER | IQTCKSRPEK | TKYFKDFLDS | WRKFHSALHQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KEKDVTDSFY | PAMRLILPQL | ERERMAYGIK | ETMLAKLYIE | LLNLPKDGKD | AVKLLNYRTP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TGSRGDAGDF | AMIAYFVLKP | RSPKRGRLTV | EQVNELLDAI | ANNNAAKNKG | LVKKSLLQLI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TQSTALEQKW | LIRMIIKDLK | LGVSQQTIFS | IFHPDAAELH | NVTTDLEKVC | RQLHDPSVSL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SDVSIMLFSA | FKPMLAAIAD | VQQIEKQMNN | QVFYIETKLD | GERMQMHKDG | DVYKYFSRNG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FDYTQQFGAS | PVDGSLTPFI | HNVFKSDIQN | CILDGEMMAY | NPETQTFMQK | GNKFDIKRMV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EDSDLQTCFC | VFDVLMINDQ | KLAHESLSKR | YKILSNVFTP | LTGRIHVVHK | KSARTRKEVI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DALNEAIDNR | EEGIMVKDPM | STYKPDKRGE | GWLKIKPEYV | NGLMDELDLL | IVGGYWGKGS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RGGMMSHFLC | AVAETPAPNE | KPTVFHSICR | VGSGYTMKEL | YDLGLKLAKH | WKPYNRKDPP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CNILCGTEKP | EMYIEPCNSV | IVQIKAAEIV | NSDMYKTDCT | LRFPRIEKIR | EDKEWYECMT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LDMLEHLRSR | AEGKLASKHL | YIDEYDEPQE | KKRRTVPKVK | KVIGIAEQFK | APDLSNVNKV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SSMFEDVEFC | VMTGMGRYSK | SELESRIAEC | GGSVVQNPGP | DTYCVIVGAE | NVRVKNIIAS |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NKYDVVKAEW | LLQCFQSKML | VPWQPAFMIH | MSPETREHFA | REYDCYGDSY | TADTDVAQLK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EVFSRVKDNK | KMPLDLIAEL | EERYSWNSCK | LCIFRGNTIY | VDYYAIINKP | STKIHGTRLS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IRALELRFYG | AKVVPLLEEG | VSHVVIGEDH | SRVKEMKALR | RMFGKKFKIV | SELWVTESVK |
| 910 | |||||
| EGVPKNETQF | LI |